Purification and Properties of an A-Amylase Produced by a Cassava-Fermenting Strain of Micrococcus Luteus
An extracellular α-amylase produced by a cassava-fermenting strain of Micrococcus luteus was purified 26-fold by gel filtration and ion-exchange chromatography. The molar mass was estimated to be approximately 56 kDa. The optimum temperature of the enzyme was 30oC, optimum pH 6.0 and optimum substrate concentration was 0.6 % (w/v). Treatment of the enzyme at 70 oC for 10 min resulted in 70 % loss of activity. The activation energy was determined to be 34.8 kj/mol. The activity of the enzyme was enhanced by Mg2+, Ca2+, K+, Na+ and inhibited by EDTA, KCN and citric acid. The enzyme may find some application in local food processing.